2026-09-18T22:58:32Z https://www.ideals.illinois.edu/oai-pmh

oai:www.ideals.illinois.edu:2142/25638 2023-07-10 col_2142_8859 col_2142_5131 com_2142_8858 com_2142_234 com_2142_5130

Frauenfelder, Hans Nordlund, Thomas Michael 2011-07-05T14:39:54Z 2011-07-05T14:39:54Z 10000-01-01 1977 Binding of carbon monoxide to a variety of heme proteins is a multistep process and can be described by a sequence of activation barriers. In the separated alpha and beta chains of hemoglobin three barriers are found which are sensitive to the structural differences between the two chains. The barriers in the beta chain change when two cysteine amino acids are modified with a mercury compound. Three processes are also observed in CO binding to cytochrome P4S0 and rates depend strongly upon the presence of the enzyme's substrate, camphor. Comparisons among these and other heme proteins and compounds show that protein structure can influence any of the activation barriers. Submitted by Carolyn Mead (cmead2@illinois.edu) on 2011-07-05T14:39:54Z No. of bitstreams: 1 1977_nordlund.pdf: 2278025 bytes, checksum: 30d856cf0e272f68cc5f9fa546c9ae06 (MD5) Made available in DSpace on 2011-07-05T14:39:54Z (GMT). No. of bitstreams: 1 1977_nordlund.pdf: 2278025 bytes, checksum: 30d856cf0e272f68cc5f9fa546c9ae06 (MD5) Previous issue date: 1977 Restriction data tranferred 2014-07-01T11:32:29-05:00 Original Data Group with Access UIUC Users [automated] Release Date: none Reason: Thesis Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Carolyn Mead (cmead2@illinois.edu) on 2011-07-05T14:39:54Z Item is restricted indefinitely. Thesis U of I Only 1939804 http://hdl.handle.net/2142/25638 en 1977 Thomas Michael Nordlund heme proteins heme protein structure ligand binding carbon monoxide binding hemoglobin Heme protein structure and ligand binding Dissertation / Thesis text Physics Physics University of Illinois at Urbana-Champaign Dissertation Ph.D.